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重组日本血吸虫副肌球蛋白的表达与纯化
引用本文:周金春,易新元,Kalinna BH.重组日本血吸虫副肌球蛋白的表达与纯化[J].中南大学学报(医学版),2000,25(2):106-108.
作者姓名:周金春  易新元  Kalinna BH
作者单位:湖南医科大学血吸虫病研究!长沙410078,湖南医科大学血吸虫病研究!长沙410078,The Queensland Institute of Medical Research!Queensland 4029,Australia,The Queensland Institute of Medical Research!Queensland 4029,Australia
基金项目:WHO/TDR资助! ( 980 2 6 8)
摘    要:用基因重组技术 ,将日本血吸虫副肌球蛋白 (rSj97)基因亚克隆至表达载体pQE30上。在IPTG诱导下 ,重组日本血吸虫副肌球蛋白在大肠杆菌中得以高效表达。通过快速蛋白质液相色谱仪 (FPLC) ,经TALON柱和离子交换柱两步分离纯化 ,获得大量高纯度的重组日本血吸虫副肌球蛋白 ,为水牛现场试验提供了充足的抗原

关 键 词:日本血吸虫    副肌球蛋白    抗原纯化  

Expression and purification of recombinant Schistosoma japonicum paramyosin~①
Kalinna BH.Expression and purification of recombinant Schistosoma japonicum paramyosin~①[J].Journal of Central South University (Medical Sciences)Journal of Central South University (Medical Sciences),2000,25(2):106-108.
Authors:Kalinna BH
Institution:1Department of Parasitology, Hunan Medical University(Changsha 410078); 2The Queensland Institute of Medical Research(Queensland 4029, Australia
Abstract:Paramyosin of Schistosoma japonicum was expressed at a high level in E.coli. The recombinant protein could be easily purified from bacteria lysate by fast protein liquid chromatography(FPLC) on a TALON resin column, due to the protein being expressed with a tag of six histidine residue fused to the N terminus. The protein was completely soluble and could be eluted under non denaturing condition using imidazole. To eliminate imidazole and residue of E.coli, the elution was further purified by ion exchange chromatography. The purified protein will be used in water buffaloes in the study on protective immunity against Schistosoma japonicum.
Keywords:Schistosoma japonicum  paramyosin  antigen purification~*  gene recombination
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